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Coatomer

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Mouse COPI coat complex containing subunits alpha (grey), beta (green), beta prime (pink), delta (yellow), gamma-1 (red), zeta-1 (aqua) and protein Arf-1 (cyan) (PDB entry 5nzu)

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Coatomers (COPI) are a set of vesicles' coating proteins ^[1]. Coatomers contain several subunits which are named according to decreasing molecular weight as alpha, beta', gamma, delta, epsilon and zeta-1. Protein ADP-ribosylation factor 1 (Arf-1) is part of the vesicle-coating complex^[2].

1 Function
2 Disease
3 Structural highlights
4 Coatomer 3D structures
5 References

Function

COPI function in the sorting and trafficking of proteins between sub cellular organelles ^[3]. COP1 induces membrane curvature during budding^[4]. Dilysine motifs on transmembrane proteins are recognised by COPI alpha and beta' subunits and packaged into COPI-coated vesicles for transport from Golgi to ER^[5].

Disease

Mutations in COPI can result in osteoporosis, fractures and developmental delays. Deficiency in COPI alpha subunit cause COPA syndrome^[6].

Structural highlights

The consists of subunit alpha, subunit beta, subunit beta', subunit gamma-1, subunit delta, subunit zeta-1 and protein Arf-1^[7].

Coatomer 3D structures

References

↑ Waters MG, Serafini T, Rothman JE. 'Coatomer': a cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles. Nature. 1991 Jan 17;349(6306):248-51. PMID:1898986 doi:10.1038/349248a0
↑ Lippincott-Schwartz J, Cole NB, Donaldson JG. Building a secretory apparatus: role of ARF1/COPI in Golgi biogenesis and maintenance. Histochem Cell Biol. 1998 May-Jun;109(5-6):449-62. PMID:9681627 doi:10.1007/s004180050247
↑ Marom R, Burrage LC, Venditti R, Clément A, Blanco-Sánchez B, Jain M, Scott DA, Rosenfeld JA, Sutton VR, Shinawi M, Mirzaa G, DeVile C, Roberts R, Calder AD, Allgrove J, Grafe I, Lanza DG, Li X, Joeng KS, Lee YC, Song IW, Sliepka JM, Batkovskyte D, Washington M, Dawson BC, Jin Z, Jiang MM, Chen S, Chen Y, Tran AA, Emrick LT, Murdock DR, Hanchard NA, Zapata GE, Mehta NR, Weis MA, Scott AA, Tremp BA, Phillips JB, Wegner J, Taylor-Miller T, Gibbs RA, Muzny DM, Jhangiani SN, Hicks J, Stottmann RW, Dickinson ME, Seavitt JR, Heaney JD, Eyre DR, Westerfield M, De Matteis MA, Lee B. COPB2 loss of function causes a coatopathy with osteoporosis and developmental delay. Am J Hum Genet. 2021 Sep 2;108(9):1710-1724. PMID:34450031 doi:10.1016/j.ajhg.2021.08.002
↑ Beck R, Prinz S, Diestelkötter-Bachert P, Röhling S, Adolf F, Hoehner K, Welsch S, Ronchi P, Brügger B, Briggs JA, Wieland F. Coatomer and dimeric ADP ribosylation factor 1 promote distinct steps in membrane scission. J Cell Biol. 2011 Sep 5;194(5):765-77. PMID:21893600 doi:10.1083/jcb.201011027
↑ Ma W, Goldberg J. Rules for the recognition of dilysine retrieval motifs by coatomer. EMBO J. 2013 Mar 12. doi: 10.1038/emboj.2013.41. PMID:23481256 doi:http://dx.doi.org/10.1038/emboj.2013.41
↑ Kumrah R, Mathew B, Vignesh P, Singh S, Rawat A. Genetics of COPA syndrome. Appl Clin Genet. 2019 Feb 8;12:11-18. PMID:30804679 doi:10.2147/TACG.S153600
↑ Dodonova SO, Aderhold P, Kopp J, Ganeva I, Rohling S, Hagen WJH, Sinning I, Wieland F, Briggs JAG. 9A structure of the COPI coat reveals that the Arf1 GTPase occupies two contrasting molecular environments. Elife. 2017 Jun 16;6. pii: e26691. doi: 10.7554/eLife.26691. PMID:28621666 doi:http://dx.doi.org/10.7554/eLife.26691